Abstract
The strain of Mycobacterium sp. VKM Ac-1817D forms 9α-hydroxy-androst-4-ene-3,17-dione (9-OH-AD) as a major product from sitosterol. The formation of 9-OH-AD was accompanied with its partial destruction due to residual steroid-1-dehydrogenase (St1DH) activity. The activity was found to be induced by androst-4-ene-3,17-dione (AD), while other intermediates of sitosterol oxidation did not influence 1(2)-dehydrogenation. The enzyme is located mainly in the cytosolic fraction. The cytosolic St1DH (dimer, M r∼58 kDa) was partially purified by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-Sepharose and Phenyl-Sepharose, and gel filtration on Bio-Gel A-0.5M. It expressed the St1DH activity toward both AD and 9-OH-AD.
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Sukhodolskaya, G.V., Nikolayeva, V.M., Khomutov, S.M. et al. Steroid-1-dehydrogenase of Mycobacterium sp. VKM Ac-1817D strain producing 9α-hydroxy-androst-4-ene-3,17-dione from sitosterol. Appl Microbiol Biotechnol 74, 867–873 (2007). https://doi.org/10.1007/s00253-006-0728-4
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DOI: https://doi.org/10.1007/s00253-006-0728-4